scholarly journals Activation of pyk2/Related Focal Adhesion Tyrosine Kinase and Focal Adhesion Kinase in Cardiac Remodeling

2002 ◽  
Vol 277 (47) ◽  
pp. 45203-45210 ◽  
Author(s):  
Jaime Melendez ◽  
Sara Welch ◽  
Erik Schaefer ◽  
Christine S. Moravec ◽  
Shalom Avraham ◽  
...  
1995 ◽  
Vol 270 (36) ◽  
pp. 21206-21219 ◽  
Author(s):  
Hiroko Sasaki ◽  
Kazuko Nagura ◽  
Masaho Ishino ◽  
Hirotoshi Tobioka ◽  
Kiyoshi Kotani ◽  
...  

1997 ◽  
Vol 110 (4) ◽  
pp. 401-407 ◽  
Author(s):  
D. Ilic ◽  
C.H. Damsky ◽  
T. Yamamoto

Morphogenetic processes during development, including cell migration, depend on signals from both the extracellular matrix (ECM) and soluble signaling factors. Extensive evidence has shown that the nonreceptor tyrosine kinase, focal adhesion kinase (FAK), is activated in response to both kind of signal. The most definitive evidence that FAK is directly downstream of signals initiated by the ECM comes from comparing the phenotypes of mice deficient for FAK and the ECM molecule, fibronectin: in both cases embryos die at about E8.5 and display almost identical severe vascular and other mesodermal defects. It is now clear that there are additional FAK-like proteins, indicating the existence of a FAK family. Furthermore, FAK is not located at adhesive sites in all cells where it is expressed. This, plus extensive data indicating that FAK becomes activated in response to several soluble signaling factors, suggests that the FAK family may be at the crossroads of multiple signaling pathways that affect cell and developmental processes.


The Analyst ◽  
2017 ◽  
Vol 142 (15) ◽  
pp. 2713-2716 ◽  
Author(s):  
Nur P. Damayanti ◽  
Kevin Buno ◽  
Nagarajan Narayanan ◽  
Sherry L. Voytik Harbin ◽  
Meng Deng ◽  
...  

Focal adhesion kinase (FAK) is a cytoplasmic non-receptor tyrosine kinase essential for a diverse set of cellular functions. FAK FLIM-peptide biosensor enables real-time monitoring of FAK phopshorylation activity.


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